PXD008271

PXD008271 is an original dataset announced via ProteomeXchange.

Title	Time- and Polarity-dependent Proteomic Changes associated with Homeostatic Scaling at Central Synapses
Description	In homeostatic scaling, the cellular mechanisms that detect the offset from the set-point, the duration of the offset and implement a cellular response are not well-understood. To understand the time-dependent dynamics,we manipulated activity for 2 hrs to induce the process of up or down-scaling and metabolically labelled nascent proteins using BONCAT. We analyzed the newly synthesized proteins that exhibited significant increases or decreases in expression in response to activity manipulations and identified 168 proteins. Then, to obtain a temporal trajectory of the cellular response, we compared the proteins synthesized within 2 and 24 hrs of an activity manipulation. Surprisingly, there was little overlap in the significantly regulated newly synthesized proteins identified in the early- and late-response datasets. There was, however, overlap in the functional categories that are modulated early and late, indicating that within protein function groups, different proteomic choices can be made to effect early and late homeostatic responses.
HostingRepository	PRIDE
AnnounceDate	2018-02-16
AnnouncementXML	Submission_2018-02-16_06:25:01.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Julian Langer
SpeciesList	scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116;
ModificationList	carbamoylated residue; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; deamidated residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2017-11-23 00:16:28	ID requested
1	2018-02-16 02:10:01	announced
⏵ 2	2018-02-16 06:25:03	announced	Updated publication reference for PubMed record(s): 29447110.

Schanzenb, ä, cher CT, Langer JD, Schuman EM, Time- and polarity-dependent proteomic changes associated with homeostatic scaling at central synapses. Elife, 7():(2018) [pubmed]

curator keyword: Biological

submitter keyword: Homeostatic scaling, proteomics, BONCAT

Julian David Langer
contact affiliation	Max Planck Institute of Biophysics and Max Planck Institute for Brain Research
contact email	julian.langer@biophys.mpg.de
lab head
Julian Langer
contact affiliation	MPIs for Biophysics and Brain Research
contact email	julian.langer@biophys.mpg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2018/02/PXD008271

PRIDE project URI

• PRIDE
  1. PXD008271
     1. Label: PRIDE project
     2. Name: Time- and Polarity-dependent Proteomic Changes associated with Homeostatic Scaling at Central Synapses